Evidence map›Paper›PMID 39738953›Full record

ReviewSub-cellular biochemistry2024

Assembly of Structurally Simple Icosahedral Viruses.

Alberto López-Bueno, Jon Gil-Ranedo, José M Almendral

Abstract readReview
PubMed Publisher
In one paragraph

Review in Sub-cellular biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Alberto López-BuenoCentro de Biología Molecular "Severo Ochoa" (CSIC-UAM) and Department of Molecular Biology, Universidad Autónoma de Madrid, Madrid, Spain.
Jon Gil-RanedoFaculty of Health: Medicine, Dentistry and Human Sciences, University of Plymouth, Plymouth, UK.
José M AlmendralCentro de Biología Molecular "Severo Ochoa" (CSIC-UAM) and Department of Molecular Biology, Universidad Autónoma de Madrid, Madrid, Spain. jmalmendral@cbm.csic.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Icosahedral viruses exhibit elegant pathways of capsid assembly and maturation regulated by symmetry principles. Assembly is a dynamic process driven by consecutive and genetically programmed morphogenetic interactions between protein subunits. The non-symmetric capsid subunits are gathered by non-covalent contacts and interactions in assembly intermediates, which serve as blocks to build a symmetric capsid. In some virus examples, the assembly of the protein shell further requires non-symmetric interactions among intermediates to fold into specific conformations. In this chapter, the morphogenesis of some small and structurally simple icosahedral viruses, including representative members of the parvoviruses, picornaviruses, and polyomaviruses as paradigms, is described in some detail. Despite their small size, the assembly of these icosahedral viruses may follow rather complex pathways, as they may occur in different subcellular compartments, involve a panoply of cellular and viral factors, and regulatory protein post-translational modifications that challenge its comprehensive understanding. Mechanisms of viral genome encapsidation may imply direct interactions between the genome and the assembly intermediates, or active packaging into a preformed empty capsid. Further, membranes and factors at specific subcellular compartments may also be critically required for virus maturation. The high stability of intermediates and the process of viral maturation contribute to the overall irreversible character of the assembly process. These and other small, structurally less complex icosahedral viruses were pioneer models to understand basic principles of virus assembly, continue to be leading subjects of morphogenetic analyses, and have inspired ongoing studies on the assembly of larger, structurally more complex viruses as well as cellular and synthetic macromolecular complexes.

Indexed as

Virus AssemblyAnimalsCapsidCapsid ProteinsHumansParvovirusPicornaviridaePolyomavirusCapsid ProteinsAssembly intermediateGenome encapsidationIcosahedral capsidMaturation cleavageNuclear translocationNucleationProtein foldingProtein phosphorylationProtein–protein interactionsTriangulation numberVirus factory

Identifiers

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.